Heat Shock 70kDa protein 5 Recombinant Protein | HSPA5 recombinant protein

Recombinant Human Heat Shock 70kDa protein 5

Cat. Num. AAA144355

• Gene Names: HSPA5; BIP; MIF2; GRP78; HEL-S-89n
• Purity: Greater than 90.0% as determined by SDS-PAGE.
• Synonyms: Heat Shock 70kDa protein 5; Recombinant Human Heat Shock 70kDa protein 5; HSPA5 Human; Heat Shock 70kDa Protein 5 Human Recombinant; BIP; MIF2; GRP78; FLJ26106; HSPA5; 78 kDa glucose-regulated protein; GRP 78; Heat shock 70 kDa protein 5; Immunoglobulin heavy chain-binding protein; Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78; HSPA5 recombinant protein

• Host: E Coli
• Purity/Purification: Greater than 90.0% as determined by SDS-PAGE.
• Form/Format: The HSPA5 protein solution contains 20mM Tris-HCl, pH-8 & 10% Glycerol.; Sterile filtered colorless solution.
• Sequence: MEEDKKEDVG TVVGIDLGTT YSCVGVFKNG RVEIIANDQG NRITPSYVAF TPEGERLIGD AAKNQLTSNP ENTVFDAKRL IGRTWNDPSV QQDIKFLPFK VVEKKTKPYI QVDIGGGQTK TFAPEEISAM VLTKMKETAE AYLGKKVTHA VVTVPAYFND AQRQATKDAG TIAGLNVMRI INEPTAAAIA YGLDKREGEK NILVFDLGGG TFDVSLLTID NGVFEVVATN GDTHLGGEDF DQRVMEHFIK LYKKKTGKDV RKDNRAVQKL RREVEKAKRA LSSQHQARIE IESFYEGEDF SETLTRAKFE ELNMDLFRST MKPVQKVLED SDLKKSDIDE IVLVGGSTRI PKIQQLVKEF FNGKEPSRGI NPDEAVAYGA AVQAGVLSGD QDTGDLVLLD VCPLTLGIET VGGVMTKLIP RNTVVPTKKS QIFSTASDNQ PTVTIKVYEG ERPLTKDNHL LGTFDLTGIP PAPRGVPQIE VTFEIDVNGI LRVTAEDKGT GNKNKITITN DQNRLTPEEI ERMVNDAEKF AEEDKKLKER IDTRNELESY AYSLKNQIGD KEKLGGKLSS EDKETMEKAV EEKIEWLESH QDADIEDFKA KKKELEEIVQ PIISKLYGSA GPPPTGEEDT AELEHHHHHH
• Sequence Length: 654

• Preparation and Storage: Store at 4 degree C if entire vial will be used within 2-4 weeks. Store, frozen at -20 degree C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

Related Product Information for HSPA5 recombinant protein

Description: Recombinant Human HSPA5 produced in E Coli is a single,non-glycosylated polypeptide chain containing 640 amino acids (20-650 a.a.) and having a molecular mass of 71kDa. HSPA5 human recombinant is fused to an 8 amino acid His Tag at C-terminus and purified by convential chromatogrpahy techniques.

Introduction: Once Chinese hamster K12 cells are starved from glucose, the synthesis of GRP (glucose-regulated protein) expressed. HSPA5 also called BiP, is part of the HSP70 family and plays a role in the folding and assembly of proteins in the endoplasmic reticulum. HSPA5 plays a key role in monitoring protein transport through the cell. HSPA5 is a stress response protein which is induced by agents or conditions that adversely affect endoplasmic reticulum function. HSPA5 is crucial for the proper glycosylation, folding as well as for the maintenance of cell homeostasis and the prevention of apoptosis. HSPA5 is differentially expressed in the dorsolateral prefrontal cortex from patients with schizophrenia. HSPA5 guides posttranslational hepatitis B virus large envelope protein import into the mammalian ER. HSPA5 actively regulates multiple malignant phenotypes, including cell growth, migration, and invasion.

Product Categories/Family for HSPA5 recombinant protein

Heat Shock Proteins; Recombinant Proteins; Heat Shock Protein

NCBI and Uniprot Product Information

• NCBI GI #: 16507237
• NCBI GeneID: 3309
• NCBI Accession #: NP_005338.1
• NCBI GenBank Nucleotide #: NM_005347.4
• UniProt Accession #: P11021; Q2EF78; Q9NPF1; Q9UK02; B0QZ61
• Molecular Weight: 72,333 Da
• NCBI Official Full Name: 78 kDa glucose-regulated protein
• NCBI Official Synonym Full Names: heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa)
• NCBI Official Symbol: HSPA5
• NCBI Official Synonym Symbols: BIP; MIF2; GRP78; HEL-S-89n
• NCBI Protein Information: 78 kDa glucose-regulated protein; endoplasmic reticulum lumenal Ca(2+)-binding protein grp78; epididymis secretory sperm binding protein Li 89n; immunoglobulin heavy chain-binding protein
• UniProt Protein Name: 78 kDa glucose-regulated protein
• UniProt Gene Name: HSPA5
• UniProt Synonym Gene Names: GRP78; GRP-78; BiP
• UniProt Entry Name: GRP78_HUMAN

NCBI Description

The protein encoded by this gene is a member of the heat shock protein 70 (HSP70) family. It is localized in the lumen of the endoplasmic reticulum (ER), and is involved in the folding and assembly of proteins in the ER. As this protein interacts with many ER proteins, it may play a key role in monitoring protein transport through the cell.[provided by RefSeq, Sep 2010]

Uniprot Description

GRP78: a member of the HSP family of molecular chaperones required for endoplasmic reticulum integrity and stress-induced autophagy. Plays a central role in regulating the unfolded protein response (UPR), and is an obligatory component of autophagy in mammalian cells. May play an important role in cellular adaptation and oncogenic survival. One of the client proteins of GRP78 is protein double-stranded RNA-activated protein-like endoplasmic reticulum kinase (PERK). Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER.

Protein type: Chaperone; Heat shock protein

Chromosomal Location of Human Ortholog: 9q33.3

Cellular Component: signalosome; endoplasmic reticulum membrane; focal adhesion; cell surface; smooth endoplasmic reticulum; mitochondrion; endoplasmic reticulum lumen; endoplasmic reticulum; ER-Golgi intermediate compartment; membrane; plasma membrane; melanosome; integral to endoplasmic reticulum membrane; midbody; nucleus

Molecular Function: protein domain specific binding; protein binding; enzyme binding; ubiquitin protein ligase binding; chaperone binding; unfolded protein binding; ATPase activity; ribosome binding; misfolded protein binding; calcium ion binding; glycoprotein binding; ATP binding

Biological Process: platelet activation; ER-associated protein catabolic process; cerebellum structural organization; unfolded protein response; cerebellar Purkinje cell layer development; cellular response to glucose starvation; substantia nigra development; platelet degranulation; unfolded protein response, activation of signaling protein activity; cellular protein metabolic process; positive regulation of protein ubiquitination; negative regulation of transforming growth factor beta receptor signaling pathway; blood coagulation; ER overload response; negative regulation of apoptosis; positive regulation of cell migration